about
Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociationType 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coliStructural basis of type 2A von Willebrand disease investigated by molecular dynamics simulations and experimentsYielding elastic tethers stabilize robust cell adhesionUncoiling mechanics of Escherichia coli type I fimbriae are optimized for catch bondsTight Conformational Coupling between the Domains of the Enterotoxigenic Escherichia coli Fimbrial Adhesin CfaE Regulates Binding State TransitionBacterial adhesion to target cells enhanced by shear forceShear-dependent 'stick-and-roll' adhesion of type 1 fimbriated Escherichia coliFor catch bonds, it all hinges on the interdomain region: Figure 1.Mechanism of allosteric propagation across a β-sheet structure investigated by molecular dynamics simulations.Catch-bond model derived from allostery explains force-activated bacterial adhesion.Elevated shear stress protects Escherichia coli cells adhering to surfaces via catch bonds from detachment by soluble inhibitors.Weak rolling adhesion enhances bacterial surface colonization.Shear-enhanced binding of intestinal colonization factor antigen I of enterotoxigenic Escherichia coli.Computation of conformational coupling in allosteric proteinsFimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.Shear-stabilized rolling behavior of E. coli examined with simulations.Biophysics of catch bonds.Catch bonds in adhesion.Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coliInactive conformation enhances binding function in physiological conditionsDifferential surface activation of the A1 domain of von Willebrand factor.Adaptive mutations in the signal peptide of the type 1 fimbrial adhesin of uropathogenic Escherichia coliAllosteric coupling in the bacterial adhesive protein FimHCatch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?Conformational inactivation induces immunogenicity of the receptor-binding pocket of a bacterial adhesin.Mechanochemistry of receptor-ligand bonds.Catch bond-mediated adhesion without a shear threshold: trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli.A structural model for force regulated integrin binding to fibronectin's RGD-synergy site.Beyond induced-fit receptor-ligand interactions: structural changes that can significantly extend bond lifetimes.Integrin-like allosteric properties of the catch bond-forming FimH adhesin of Escherichia coli.A multiplexed magnetic tweezer with precision particle tracking and bi-directional force control.Specific electrostatic interactions between charged amino acid residues regulate binding of von Willebrand factor to blood platelets.Only the strong: when antibodies hold on.Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.Serine-Rich Repeat Adhesins Mediate Shear-Enhanced Streptococcal Binding to Platelets.The cysteine bond in the Escherichia coli FimH adhesin is critical for adhesion under flow conditionsDistinctive features of the biological catch bond in the jump-ramp force regime predicted by the two-pathway modelThe catch bond mechanism between von Willebrand factor and platelet surface receptors investigated by molecular dynamics simulationsCalpain drives pyroptotic vimentin cleavage, intermediate filament loss, and cell rupture that mediates immunostimulation
P50
Q24303908-104006FC-4196-4AE6-8C9D-F0DEDEF0233CQ24635242-219B46C4-5DC5-4A53-991B-682912C43A14Q27318490-96254651-7BE1-4D5E-91A9-0A0CA480C12AQ27320178-693F2E67-E916-4C4D-8423-B5D67698C32AQ27335234-FB17C84E-CDCE-49BF-AD35-FE748DE29E19Q27676231-ED63FCD8-B651-46EB-B099-2B22C900CDA7Q28214001-F68F5858-07DA-45E5-8BAE-746449AF3812Q28283793-73ACF9C1-DE71-4D7E-B587-089B3F2F8C1BQ29026706-040DDBC5-8EDF-4BDD-91E5-F528EB760494Q30387043-5513A990-E4B5-49F3-B41A-5A00E49F2E07Q30445371-70D0A230-B970-4F6A-8B14-4E2CAF4E4FB7Q30477190-587EB21C-FE8C-47E7-9D8B-4ECE917093F2Q30479341-C48B9921-27D3-4C0F-8700-DDB15EA2268AQ30496306-65159215-0A79-422C-A3CF-ED3BD8A5C1D9Q30872872-1E136F99-C4C2-4ABD-AAF9-6318E9B0F80FQ33320807-DCB53F87-7AA7-4CDA-A1E8-A51322CD4319Q34206072-E79EC5A3-5897-4634-B2F4-32DAB7EF9EE1Q34788335-1874D412-5FA6-4531-BE20-B2670B722761Q34799204-DF050166-4DEB-4DC2-A4A7-F0BA40BA219CQ35606583-34149CFE-C4E7-472D-B3E2-B9A7FF756606Q35961228-003F6B57-4AC0-4F3B-9C32-DF1384CA1E39Q36678324-C274C9E1-9EE3-45CD-AE39-5581A69B2397Q36825331-005DCB19-E424-453F-AE1B-97885D39BCBCQ37099778-1A1488D4-D824-4BEC-AFF0-06B324E5769CQ37293577-16ABB98C-ECC3-4A5C-9ED1-285C0D7D1F01Q37340809-D8E4C01A-954E-4C21-8A0C-492CE8770AE0Q37373858-D7E6CC6F-D803-47D8-BB7C-C2CAEFB0A64FQ38314107-FF4D45B7-D71F-408A-A98A-599852AA5B77Q45711560-4D9BCE97-89C6-4911-B64D-8FD105CEDE1FQ46494878-C1DA4E11-2703-40DC-8582-4744C045071EQ46824098-30EE427E-871F-409E-A331-2C4DF335888DQ47099312-BFB719AF-7B04-454A-8335-D013CC7123B2Q47661600-8153E8BB-7258-42B0-91C6-76268A859E98Q49960888-535864AF-6B33-4761-9216-687D920D2E14Q52579774-9EF0C101-7D84-4449-A820-1CE170A5F940Q54247887-AA04B0F5-B95E-41E5-AE78-37694D9B58FEQ57393699-E0334A5B-D148-40FE-8F13-A64F17586496Q81029280-719E127C-D7C9-4FFF-8FCF-8B7B47B63CDCQ84523995-66FD733B-E60B-48A7-917B-C20BF0E13E09Q91843783-EBD33E94-46DA-4162-9DAD-B7CF696DEF39
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Wendy Thomas
@ast
Wendy Thomas
@en
Wendy Thomas
@es
Wendy Thomas
@nl
Wendy Thomas
@sl
type
label
Wendy Thomas
@ast
Wendy Thomas
@en
Wendy Thomas
@es
Wendy Thomas
@nl
Wendy Thomas
@sl
prefLabel
Wendy Thomas
@ast
Wendy Thomas
@en
Wendy Thomas
@es
Wendy Thomas
@nl
Wendy Thomas
@sl
P106
P31
P496
0000-0001-8602-0819